Abstract:
:The crystal structure of the tetrameric DNA-binding domain of the single-stranded DNA binding protein from Escherichia coli was determined at a resolution of 2.9 A using multiwavelength anomalous dispersion. Each monomer in the tetramer is topologically similar to an oligomer-binding fold. Two monomers each contribute three beta-strands to a single six-stranded beta-sheet to form a dimer. Two dimer-dimer interfaces are observed within the crystal. One of these stabilizes the tetramer in solution. The other interface promotes a superhelical structure within the crystal that may reflect tetramer-tetramer interactions involved in the positive cooperative binding of the single-stranded DNA-binding protein to single-stranded DNA.
journal_name
Proc Natl Acad Sci U S Aauthors
Raghunathan S,Ricard CS,Lohman TM,Waksman Gdoi
10.1073/pnas.94.13.6652subject
Has Abstractpub_date
1997-06-24 00:00:00pages
6652-7issue
13eissn
0027-8424issn
1091-6490journal_volume
94pub_type
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